this with annotations you find in gene/protein databases, but these can be outdated or inaccurate. Falcon Edison Scientific Literature 31 citations 1 artifacts 2026-07-06T17:24:13.128211
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The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

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Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Comprehensive Research Report: fmc1 (SPAC1486.11) in Schizosaccharomyces pombe

Gene and Protein Identity

The fmc1 gene (synonym: new3; ORF: SPAC1486.11; UniProt: G2TRM0) encodes the ATP synthase assembly factor Fmc1, mitochondrial (also known as Formation of Mitochondrial Complexes protein 1), in Schizosaccharomyces pombe (fission yeast, strain 972 / ATCC 24843). The protein belongs to the FMC1 family and contains a Complex1_LYR_2 domain (PF13233/IPR039196), classifying it within the mitochondrial LYRM (LYR motif-containing) protein superfamily.

Note on literature availability: No direct experimental studies on fmc1 in S. pombe were identified during this review. The functional annotation of the S. pombe protein is therefore inferred from the well-characterized Saccharomyces cerevisiae ortholog (FMC1/Fmc1p), supported by cross-genome bioinformatic analyses that confirm FMC1 homologs are present in both Ascomycota (including S. pombe) and Basidiomycota (pickova2005assemblyfactorsof pages 1-2, pickova2005assemblyfactorsof pages 5-7, pickova2005assemblyfactorsof pages 7-9).

The following summary table provides an overview of key properties:

Property Description
Gene name fmc1; UniProt-provided synonym new3; ORF SPAC1486.11 for the target protein in Schizosaccharomyces pombe (strain 972 / ATCC 24843) (user-provided UniProt context).
Organism (S. pombe) Schizosaccharomyces pombe (fission yeast), strain 972 / ATCC 24843; this is the correct target organism and should be distinguished from the much better studied Saccharomyces cerevisiae ortholog literature. Cross-genome analysis lists S. pombe among Ascomycota species carrying FMC1 homologs (pickova2005assemblyfactorsof pages 5-7).
UniProt ID G2TRM0 (user-provided UniProt accession for the target S. pombe protein).
S. cerevisiae ortholog FMC1 / Fmc1p, the founding and experimentally characterized fungal ortholog required for mitochondrial ATP synthase F1-sector assembly/stability under heat stress (lefebvrelegendre2001identificationofa pages 1-1, lefebvrelegendre2001identificationofa pages 6-7).
Protein name ATP synthase assembly factor Fmc1, mitochondrial; also called Formation of mitochondrial complexes protein 1. In S. cerevisiae, Fmc1p is a small, nuclear-encoded mitochondrial protein involved in ATP synthase biogenesis (lefebvrelegendre2001identificationofa pages 1-1, lefebvrelegendre2001identificationofa pages 4-5).
Molecular function Best-supported function is as an assembly/stability factor for the F1 sector of mitochondrial ATP synthase (Complex V), especially under elevated temperature. It is not a catalytic enzyme; rather, it acts as an accessory/chaperone-like factor helping productive F1 assembly and preventing aggregation of F1 α/β subunits, likely through supporting Atp12p folding/stability/function (lefebvrelegendre2001identificationofa pages 1-1, lefebvrelegendre2001identificationofa pages 6-7, rak2009assemblyoff0 pages 2-3, lefebvrelegendre2001identificationofa pages 5-6).
Subcellular localization In S. cerevisiae, Fmc1p is a soluble mitochondrial matrix protein, imported as a precursor with an N-terminal targeting presequence; it is either free in the matrix or loosely associated with the inner face of the inner membrane (lefebvrelegendre2001identificationofa pages 4-5, lefebvrelegendre2001identificationofa pages 1-1). The S. pombe protein is annotated by UniProt as mitochondrial precursor, consistent with orthology.
Domain family Belongs to the FMC1/LYRM (Complex1_LYR_2) family of mitochondrial LYR-motif proteins. LYRM proteins typically act as accessory factors for OXPHOS complexes and mitochondrial biogenesis pathways; FMC1 is classified as a lineage-specific LYRM family member (angerer2013thesuperfamilyof pages 1-2, angerer2013thesuperfamilyof pages 4-5, pickova2005assemblyfactorsof pages 7-9).
Key interactions (Atp12p, ACPM) Atp12p: genetic and functional interaction is strong—ATP12 overexpression suppresses the fmc1Δ defect, and Fmc1p is proposed to support Atp12p folding/stability/function during F1 assembly (lefebvrelegendre2001identificationofa pages 6-7, rak2009assemblyoff0 pages 2-3, lefebvrelegendre2001identificationofa pages 5-6). ACPM: LYRM-family review reports direct association of FMC1-containing complexes with mitochondrial acyl-carrier protein (ACPM) by tandem affinity purification, linking FMC1 to broader mitochondrial biogenesis networks (angerer2013thesuperfamilyof pages 5-6, angerer2013thesuperfamilyof pages 4-5).
Phenotype of deletion (at elevated temperature) In S. cerevisiae, fmc1Δ causes severe oxidative growth defects at 37°C on non-fermentable carbon sources; ATP synthase biogenesis is strongly impaired, and F1 α/β subunits aggregate in the matrix instead of assembling into functional oligomers (lefebvrelegendre2001identificationofa pages 1-1, lefebvrelegendre2001identificationofa pages 6-7, lefebvrelegendre2001identificationofa pages 4-4, lefebvrelegendre2001identificationofa pages 2-3).
Phenotype at normal temperature Unlike ATP11 or ATP12, FMC1 is not essential under normal growth temperature (28–30°C) in budding yeast; F1 assembly can proceed sufficiently in these conditions, indicating a conditional/heat-stress requirement (lefebvrelegendre2001identificationofa pages 1-1, rak2009assemblyoff0 pages 2-3).
Conservation (fungi - Ascomycota and Basidiomycota) Comparative genomics indicates Fmc1p homologs are fungal-lineage restricted, found in Ascomycota and Basidiomycota rather than broadly across eukaryotes. The same analysis explicitly lists Schizosaccharomyces pombe among Ascomycota taxa carrying FMC1 homologs, supporting annotation of the target gene as the fungal ATP synthase assembly factor ortholog (pickova2005assemblyfactorsof pages 1-2, pickova2005assemblyfactorsof pages 5-7, pickova2005assemblyfactorsof pages 7-9).
Relevance to human disease (ATP synthase disorders) Although human cells do not use FMC1 itself as a standard disease gene analog, fmc1Δ yeast is a well-established model of ATP synthase deficiency because its primary defect is impaired F1 assembly and ATP synthesis. It has been used in drug-repurposing and pathway-modulation studies, including identification of TIM23-dependent mitochondrial protein sorting as a therapeutic intervention point and drug-drop screening campaigns of ~12,000 compounds for ATP synthase-related mitochondrial disease phenotypes (schwimmer2006yeastmodelsof pages 8-9, aiyar2014mitochondrialproteinsorting pages 1-2, aiyar2014mitochondrialproteinsorting pages 5-6, magistrati2023drugdroptest pages 5-6, magistrati2023drugdroptest pages 2-3).

Table: This table summarizes the key characteristics of the target FMC1/fmc1 protein, with emphasis on the evidence-supported function of the fungal ortholog and what can be inferred for the S. pombe protein. It is useful for quickly separating direct evidence from orthology-based inference.

1. Primary Function: Assembly Factor for the F1 Sector of Mitochondrial ATP Synthase

FMC1 was first identified and characterized in S. cerevisiae by Lefebvre-Legendre et al. (2001) as a nuclear gene encoding a protein required for the assembly and stability of the F1 sector of mitochondrial ATP synthase (F1FO-ATP synthase, Complex V) (lefebvrelegendre2001identificationofa pages 1-1, lefebvrelegendre2001identificationofa pages 1-2). The mitochondrial ATP synthase is a multisubunit complex in which the membrane-embedded FO domain conducts protons across the inner mitochondrial membrane, while the F1 domain (comprising an α₃β₃γδε hexamer) catalyzes ATP synthesis. FMC1 does not itself catalyze a chemical reaction; rather, it functions as an accessory assembly factor—a chaperone-like protein—that ensures the productive folding and oligomerization of the F1 α and β subunits within the mitochondrial matrix.

A distinguishing feature of FMC1 is its conditional requirement: unlike the assembly factors Atp11p and Atp12p, which are essential for F1 assembly under all growth conditions, Fmc1p is specifically required at elevated temperatures (37°C) and is dispensable for F1 assembly at normal growth temperatures (28–30°C) (lefebvrelegendre2001identificationofa pages 1-1, rak2009assemblyoff0 pages 2-3). In cells lacking Fmc1p grown at 37°C, the F1 α and β subunits are properly synthesized, imported into mitochondria, and processed to their mature size, but instead of assembling into functional F1 oligomers, they aggregate into large, insoluble inclusions in the mitochondrial matrix (lefebvrelegendre2001identificationofa pages 1-1, lefebvrelegendre2001identificationofa pages 6-7, lefebvrelegendre2001identificationofa pages 4-4).

2. Molecular Mechanism: Functional Relationship with Atp12p

The key mechanistic insight into FMC1 function comes from its functional relationship with Atp12p, a dedicated chaperone that binds to the F1 α subunit and prevents its non-productive aggregation (lefebvrelegendre2001identificationofa pages 6-7, rak2009assemblyoff0 pages 2-3, lefebvrelegendre2001identificationofa pages 7-8). Several lines of evidence demonstrate this relationship:

Based on these findings, Fmc1p has been proposed to function as a factor that assists the folding, stability, or proper functioning of Atp12p, with this requirement becoming critical under heat stress conditions when protein folding is challenged (lefebvrelegendre2001identificationofa pages 1-1, lefebvrelegendre2001identificationofa pages 7-8).

Additionally, Song et al. (2023) demonstrated a genetic interaction between fmc1Δ and the mitochondrial Hsp70 (ssc1-62) mutant. While individual ssc1-62 and fmc1Δ mutants show only mild growth defects, the double mutant exhibits severe phenotypes: growth is blocked on non-fermentable carbon sources, and ATP synthase levels are dramatically diminished, with particularly severe reductions in F1 domain levels. This indicates that mitochondrial Hsp70 (mtHsp70) and Fmc1 cooperatively function in F1FO-ATP synthase assembly (song2023themitochondrialhsp70 pages 6-7).

3. Subcellular Localization

In S. cerevisiae, Fmc1p is a soluble protein localized in the mitochondrial matrix (lefebvrelegendre2001identificationofa pages 4-5, lefebvrelegendre2001identificationofa pages 1-1). The protein is synthesized as a precursor of approximately 18.4 kDa (155 amino acids in S. cerevisiae) containing an N-terminal mitochondrial targeting presequence of approximately 4 kDa, which is cleaved upon import into the matrix (lefebvrelegendre2001identificationofa pages 4-5). Biochemical fractionation experiments confirmed its soluble nature: Fmc1p is recovered in water-soluble form after osmotic disruption of mitochondrial membranes and is protected from proteinase K degradation, indicating localization within the matrix compartment, either free or loosely associated with the inner face of the inner mitochondrial membrane (lefebvrelegendre2001identificationofa pages 4-5). The S. pombe protein (G2TRM0) is annotated by UniProt as a mitochondrial precursor, consistent with this localization pattern.

4. Domain Architecture and Membership in the LYRM Protein Superfamily

FMC1 is classified as a member of the Complex1_LYR_2 family within the broader LYRM (LYR motif-containing) protein superfamily (angerer2013thesuperfamilyof pages 1-2, angerer2013thesuperfamilyof pages 4-5). LYRM proteins are characterized by a conserved leucine/tyrosine/arginine (LYR) motif and function as accessory subunits or assembly factors for OXPHOS complexes (Complexes I, II, III, and V) (angerer2013thesuperfamilyof pages 1-2). LYRM proteins play diverse roles in mitochondrial homeostasis, including iron-sulfur (Fe-S) cluster biogenesis (e.g., LYRM4/Isd11) and connections to mitochondrial fatty acid synthesis type II pathways (angerer2013thesuperfamilyof pages 2-4).

Notably, tandem affinity purification studies in S. cerevisiae demonstrated that FMC1-containing protein complexes directly associate with ACPM (the mitochondrial acyl-carrier protein of the FAS type II pathway) (angerer2013thesuperfamilyof pages 5-6, angerer2013thesuperfamilyof pages 4-5). This interaction places FMC1 within a broader network of LYRM proteins that connect OXPHOS complex assembly with mitochondrial lipid metabolism and Fe-S cluster biogenesis pathways (angerer2013thesuperfamilyof pages 1-2, angerer2013thesuperfamilyof pages 2-4). Although FMC1 itself is not known to bind or transfer Fe-S clusters, the LYR domain may facilitate interactions with the mitochondrial biosynthetic machinery that are important for its assembly function.

5. Evolutionary Conservation

Comparative genomic analysis by Pícková et al. (2005) established that FMC1 has a restricted phylogenetic distribution compared to other F1-assembly factors. While Atp11p and Atp12p are broadly conserved across eukaryotes possessing ATP synthase, Fmc1p homologs are found specifically in Fungi, in both Ascomycota and Basidiomycota (pickova2005assemblyfactorsof pages 1-2, pickova2005assemblyfactorsof pages 7-9). This analysis explicitly includes S. pombe among the Ascomycota species carrying FMC1 homologs (pickova2005assemblyfactorsof pages 5-7). Fmc1p was not identified in Metazoa, Viridiplantae, Alveolata, or other major eukaryotic lineages, leading the authors to classify it as a "lineage-specific" assembly factor, in contrast to the "general" assembly factors Atp11p and Atp12p (pickova2005assemblyfactorsof pages 7-9). The authors propose that such lineage-specific factors may have evolved to fulfill specialized roles in individual organisms or lineages but are nonetheless important for ATP production (pickova2005assemblyfactorsof pages 7-9).

6. Biochemical and Signaling Pathway Context

FMC1 functions within the mitochondrial ATP synthase (Complex V) biogenesis pathway. The assembly of the F1 catalytic head requires several dedicated chaperones operating in the mitochondrial matrix:

Loss of Fmc1p results in a cascade of downstream effects: impaired F1 assembly leads to reduced ATP synthase accumulation, a ~90% reduction in mitochondrial ATP synthesis, and secondary effects on respiratory chain biogenesis (aiyar2014mitochondrialproteinsorting pages 1-2). The fmc1Δ phenotype demonstrates that F1 assembly is a prerequisite for complete ATP synthase maturation and proper oxidative phosphorylation.

7. Disease Relevance and Translational Applications

Although FMC1 itself has no direct human ortholog and is restricted to fungi, the fmc1Δ yeast strain has become a widely used model system for human ATP synthase disorders, including NARP syndrome (Neurogenic Ataxia and Retinitis Pigmentosa) and Leigh syndrome (schwimmer2006yeastmodelsof pages 8-9, schwimmer2006yeastmodelsof pages 6-8, aiyar2014mitochondrialproteinsorting pages 1-2, magistrati2023drugdroptest pages 5-6).

Aiyar et al. (2014) used the fmc1Δ model to screen drug repurposing libraries and identified mitochondrial protein sorting through the TIM23 complex as a therapeutic intervention point for ATP synthase disorders. Overexpression of Tim21, a regulatory subunit of the TIM23 complex, substantially restored respiratory growth in fmc1Δ mutants and improved survival in human NARP patient-derived cybrids (aiyar2014mitochondrialproteinsorting pages 5-6, aiyar2014mitochondrialproteinsorting pages 4-5). Magistrati et al. (2023) further employed the fmc1Δ strain in "drug drop test" high-throughput screening campaigns, testing approximately 12,000 compounds to identify molecules that rescue oxidative growth defects, including chlorhexidine and sodium pyrithione (magistrati2023drugdroptest pages 5-6, magistrati2023drugdroptest pages 2-3). These findings underscore the utility of FMC1 deletion models in translational research for mitochondrial diseases (schwimmer2006yeastmodelsof pages 8-9, magistrati2023drugdroptest pages 20-21).

8. Summary

The S. pombe fmc1 gene (SPAC1486.11, UniProt G2TRM0) encodes a small, soluble mitochondrial matrix protein that functions as an assembly factor for the F1 sector of mitochondrial ATP synthase. Based on extensive characterization of the S. cerevisiae ortholog, Fmc1 is not an enzyme but rather a chaperone-like accessory factor that supports the function of the F1 α-subunit assembly chaperone Atp12p, particularly under conditions of heat stress. It is a member of the LYRM protein superfamily (Complex1_LYR_2 family), associates with the mitochondrial acyl-carrier protein ACPM, and is conserved specifically within the fungal lineage. Loss of FMC1 results in aggregation of F1 α and β subunits in the matrix, severely impairing ATP synthase biogenesis and oxidative phosphorylation. While no direct experimental studies on the S. pombe protein exist, cross-genome analyses confirm that S. pombe carries an FMC1 homolog with a conserved domain architecture, and the protein's function is highly likely to be conserved as an ATP synthase assembly factor in fission yeast mitochondria.

References

  1. (pickova2005assemblyfactorsof pages 1-2): Andrea Pícková, Martin Potocký, and Josef Houštěk. Assembly factors of f1fo‐atp synthase across genomes. Proteins: Structure, 59:393-402, May 2005. URL: https://doi.org/10.1002/prot.20452, doi:10.1002/prot.20452. This article has 45 citations.

  2. (pickova2005assemblyfactorsof pages 5-7): Andrea Pícková, Martin Potocký, and Josef Houštěk. Assembly factors of f1fo‐atp synthase across genomes. Proteins: Structure, 59:393-402, May 2005. URL: https://doi.org/10.1002/prot.20452, doi:10.1002/prot.20452. This article has 45 citations.

  3. (pickova2005assemblyfactorsof pages 7-9): Andrea Pícková, Martin Potocký, and Josef Houštěk. Assembly factors of f1fo‐atp synthase across genomes. Proteins: Structure, 59:393-402, May 2005. URL: https://doi.org/10.1002/prot.20452, doi:10.1002/prot.20452. This article has 45 citations.

  4. (lefebvrelegendre2001identificationofa pages 1-1): Linnka Lefebvre-Legendre, Jacques Vaillier, Houssain Benabdelhak, Jean Velours, Piotr P. Slonimski, and Jean-Paul di Rago. Identification of a nuclear gene (fmc1) required for the assembly/stability of yeast mitochondrial f1-atpase in heat stress conditions*. The Journal of Biological Chemistry, 276:6789-6796, Mar 2001. URL: https://doi.org/10.1074/jbc.m009557200, doi:10.1074/jbc.m009557200. This article has 183 citations.

  5. (lefebvrelegendre2001identificationofa pages 6-7): Linnka Lefebvre-Legendre, Jacques Vaillier, Houssain Benabdelhak, Jean Velours, Piotr P. Slonimski, and Jean-Paul di Rago. Identification of a nuclear gene (fmc1) required for the assembly/stability of yeast mitochondrial f1-atpase in heat stress conditions*. The Journal of Biological Chemistry, 276:6789-6796, Mar 2001. URL: https://doi.org/10.1074/jbc.m009557200, doi:10.1074/jbc.m009557200. This article has 183 citations.

  6. (lefebvrelegendre2001identificationofa pages 4-5): Linnka Lefebvre-Legendre, Jacques Vaillier, Houssain Benabdelhak, Jean Velours, Piotr P. Slonimski, and Jean-Paul di Rago. Identification of a nuclear gene (fmc1) required for the assembly/stability of yeast mitochondrial f1-atpase in heat stress conditions*. The Journal of Biological Chemistry, 276:6789-6796, Mar 2001. URL: https://doi.org/10.1074/jbc.m009557200, doi:10.1074/jbc.m009557200. This article has 183 citations.

  7. (rak2009assemblyoff0 pages 2-3): Malgorzata Rak, Xiaomei Zeng, Jean-Jacques Brière, and Alexander Tzagoloff. Assembly of f0 in saccharomyces cerevisiae. Biochimica et biophysica acta, 1793 1:108-16, Jan 2009. URL: https://doi.org/10.1016/j.bbamcr.2008.07.001, doi:10.1016/j.bbamcr.2008.07.001. This article has 79 citations.

  8. (lefebvrelegendre2001identificationofa pages 5-6): Linnka Lefebvre-Legendre, Jacques Vaillier, Houssain Benabdelhak, Jean Velours, Piotr P. Slonimski, and Jean-Paul di Rago. Identification of a nuclear gene (fmc1) required for the assembly/stability of yeast mitochondrial f1-atpase in heat stress conditions*. The Journal of Biological Chemistry, 276:6789-6796, Mar 2001. URL: https://doi.org/10.1074/jbc.m009557200, doi:10.1074/jbc.m009557200. This article has 183 citations.

  9. (angerer2013thesuperfamilyof pages 1-2): Heike Angerer. The superfamily of mitochondrial complex1_lyr motif-containing (lyrm) proteins. Biochemical Society transactions, 41 5:1335-41, Oct 2013. URL: https://doi.org/10.1042/bst20130116, doi:10.1042/bst20130116. This article has 70 citations and is from a peer-reviewed journal.

  10. (angerer2013thesuperfamilyof pages 4-5): Heike Angerer. The superfamily of mitochondrial complex1_lyr motif-containing (lyrm) proteins. Biochemical Society transactions, 41 5:1335-41, Oct 2013. URL: https://doi.org/10.1042/bst20130116, doi:10.1042/bst20130116. This article has 70 citations and is from a peer-reviewed journal.

  11. (angerer2013thesuperfamilyof pages 5-6): Heike Angerer. The superfamily of mitochondrial complex1_lyr motif-containing (lyrm) proteins. Biochemical Society transactions, 41 5:1335-41, Oct 2013. URL: https://doi.org/10.1042/bst20130116, doi:10.1042/bst20130116. This article has 70 citations and is from a peer-reviewed journal.

  12. (lefebvrelegendre2001identificationofa pages 4-4): Linnka Lefebvre-Legendre, Jacques Vaillier, Houssain Benabdelhak, Jean Velours, Piotr P. Slonimski, and Jean-Paul di Rago. Identification of a nuclear gene (fmc1) required for the assembly/stability of yeast mitochondrial f1-atpase in heat stress conditions*. The Journal of Biological Chemistry, 276:6789-6796, Mar 2001. URL: https://doi.org/10.1074/jbc.m009557200, doi:10.1074/jbc.m009557200. This article has 183 citations.

  13. (lefebvrelegendre2001identificationofa pages 2-3): Linnka Lefebvre-Legendre, Jacques Vaillier, Houssain Benabdelhak, Jean Velours, Piotr P. Slonimski, and Jean-Paul di Rago. Identification of a nuclear gene (fmc1) required for the assembly/stability of yeast mitochondrial f1-atpase in heat stress conditions*. The Journal of Biological Chemistry, 276:6789-6796, Mar 2001. URL: https://doi.org/10.1074/jbc.m009557200, doi:10.1074/jbc.m009557200. This article has 183 citations.

  14. (schwimmer2006yeastmodelsof pages 8-9): Christine Schwimmer, Malgorzata Rak, Linnka Lefebvre‐Legendre, Stéphane Duvezin‐Caubet, Guillaume Plane, and Jean‐Paul di Rago. Yeast models of human mitochondrial diseases: from molecular mechanisms to drug screening. Biotechnology Journal, 1:270-281, Mar 2006. URL: https://doi.org/10.1002/biot.200500053, doi:10.1002/biot.200500053. This article has 55 citations and is from a peer-reviewed journal.

  15. (aiyar2014mitochondrialproteinsorting pages 1-2): Raeka S. Aiyar, Maria Bohnert, Stéphane Duvezin-Caubet, Cécile Voisset, Julien Gagneur, Emilie S. Fritsch, Elodie Couplan, Karina von der Malsburg, Charlotta Funaya, Flavie Soubigou, Florence Courtin, Sundari Suresh, Roza Kucharczyk, Justine Evrard, Claude Antony, Robert P. St.Onge, Marc Blondel, Jean-Paul di Rago, Martin van der Laan, and Lars M. Steinmetz. Mitochondrial protein sorting as a therapeutic target for atp synthase disorders. Nature Communications, Dec 2014. URL: https://doi.org/10.1038/ncomms6585, doi:10.1038/ncomms6585. This article has 42 citations and is from a highest quality peer-reviewed journal.

  16. (aiyar2014mitochondrialproteinsorting pages 5-6): Raeka S. Aiyar, Maria Bohnert, Stéphane Duvezin-Caubet, Cécile Voisset, Julien Gagneur, Emilie S. Fritsch, Elodie Couplan, Karina von der Malsburg, Charlotta Funaya, Flavie Soubigou, Florence Courtin, Sundari Suresh, Roza Kucharczyk, Justine Evrard, Claude Antony, Robert P. St.Onge, Marc Blondel, Jean-Paul di Rago, Martin van der Laan, and Lars M. Steinmetz. Mitochondrial protein sorting as a therapeutic target for atp synthase disorders. Nature Communications, Dec 2014. URL: https://doi.org/10.1038/ncomms6585, doi:10.1038/ncomms6585. This article has 42 citations and is from a highest quality peer-reviewed journal.

  17. (magistrati2023drugdroptest pages 5-6): Martina Magistrati, Alexandru Ionut Gilea, Maria Carla Gerra, Enrico Baruffini, and Cristina Dallabona. Drug drop test: how to quickly identify potential therapeutic compounds for mitochondrial diseases using yeast saccharomyces cerevisiae. International Journal of Molecular Sciences, 24:10696, Jun 2023. URL: https://doi.org/10.3390/ijms241310696, doi:10.3390/ijms241310696. This article has 8 citations.

  18. (magistrati2023drugdroptest pages 2-3): Martina Magistrati, Alexandru Ionut Gilea, Maria Carla Gerra, Enrico Baruffini, and Cristina Dallabona. Drug drop test: how to quickly identify potential therapeutic compounds for mitochondrial diseases using yeast saccharomyces cerevisiae. International Journal of Molecular Sciences, 24:10696, Jun 2023. URL: https://doi.org/10.3390/ijms241310696, doi:10.3390/ijms241310696. This article has 8 citations.

  19. (lefebvrelegendre2001identificationofa pages 1-2): Linnka Lefebvre-Legendre, Jacques Vaillier, Houssain Benabdelhak, Jean Velours, Piotr P. Slonimski, and Jean-Paul di Rago. Identification of a nuclear gene (fmc1) required for the assembly/stability of yeast mitochondrial f1-atpase in heat stress conditions*. The Journal of Biological Chemistry, 276:6789-6796, Mar 2001. URL: https://doi.org/10.1074/jbc.m009557200, doi:10.1074/jbc.m009557200. This article has 183 citations.

  20. (lefebvrelegendre2001identificationofa pages 7-8): Linnka Lefebvre-Legendre, Jacques Vaillier, Houssain Benabdelhak, Jean Velours, Piotr P. Slonimski, and Jean-Paul di Rago. Identification of a nuclear gene (fmc1) required for the assembly/stability of yeast mitochondrial f1-atpase in heat stress conditions*. The Journal of Biological Chemistry, 276:6789-6796, Mar 2001. URL: https://doi.org/10.1074/jbc.m009557200, doi:10.1074/jbc.m009557200. This article has 183 citations.

  21. (song2023themitochondrialhsp70 pages 6-7): Jiyao Song, Liesa Steidle, Isabelle Steymans, Jasjot Singh, Anne Sanner, Lena Böttinger, Dominic Winter, and Thomas Becker. The mitochondrial hsp70 controls the assembly of the f1fo-atp synthase. Nature Communications, Jan 2023. URL: https://doi.org/10.1038/s41467-022-35720-5, doi:10.1038/s41467-022-35720-5. This article has 25 citations and is from a highest quality peer-reviewed journal.

  22. (angerer2013thesuperfamilyof pages 2-4): Heike Angerer. The superfamily of mitochondrial complex1_lyr motif-containing (lyrm) proteins. Biochemical Society transactions, 41 5:1335-41, Oct 2013. URL: https://doi.org/10.1042/bst20130116, doi:10.1042/bst20130116. This article has 70 citations and is from a peer-reviewed journal.

  23. (schwimmer2006yeastmodelsof pages 6-8): Christine Schwimmer, Malgorzata Rak, Linnka Lefebvre‐Legendre, Stéphane Duvezin‐Caubet, Guillaume Plane, and Jean‐Paul di Rago. Yeast models of human mitochondrial diseases: from molecular mechanisms to drug screening. Biotechnology Journal, 1:270-281, Mar 2006. URL: https://doi.org/10.1002/biot.200500053, doi:10.1002/biot.200500053. This article has 55 citations and is from a peer-reviewed journal.

  24. (aiyar2014mitochondrialproteinsorting pages 4-5): Raeka S. Aiyar, Maria Bohnert, Stéphane Duvezin-Caubet, Cécile Voisset, Julien Gagneur, Emilie S. Fritsch, Elodie Couplan, Karina von der Malsburg, Charlotta Funaya, Flavie Soubigou, Florence Courtin, Sundari Suresh, Roza Kucharczyk, Justine Evrard, Claude Antony, Robert P. St.Onge, Marc Blondel, Jean-Paul di Rago, Martin van der Laan, and Lars M. Steinmetz. Mitochondrial protein sorting as a therapeutic target for atp synthase disorders. Nature Communications, Dec 2014. URL: https://doi.org/10.1038/ncomms6585, doi:10.1038/ncomms6585. This article has 42 citations and is from a highest quality peer-reviewed journal.

  25. (magistrati2023drugdroptest pages 20-21): Martina Magistrati, Alexandru Ionut Gilea, Maria Carla Gerra, Enrico Baruffini, and Cristina Dallabona. Drug drop test: how to quickly identify potential therapeutic compounds for mitochondrial diseases using yeast saccharomyces cerevisiae. International Journal of Molecular Sciences, 24:10696, Jun 2023. URL: https://doi.org/10.3390/ijms241310696, doi:10.3390/ijms241310696. This article has 8 citations.

Artifacts

Citations

  1. pickova2005assemblyfactorsof pages 5-7
  2. lefebvrelegendre2001identificationofa pages 4-4
  3. lefebvrelegendre2001identificationofa pages 4-5
  4. angerer2013thesuperfamilyof pages 1-2
  5. angerer2013thesuperfamilyof pages 2-4
  6. pickova2005assemblyfactorsof pages 7-9
  7. aiyar2014mitochondrialproteinsorting pages 1-2
  8. pickova2005assemblyfactorsof pages 1-2
  9. lefebvrelegendre2001identificationofa pages 1-1
  10. lefebvrelegendre2001identificationofa pages 6-7
  11. lefebvrelegendre2001identificationofa pages 5-6
  12. angerer2013thesuperfamilyof pages 4-5
  13. angerer2013thesuperfamilyof pages 5-6
  14. lefebvrelegendre2001identificationofa pages 2-3
  15. schwimmer2006yeastmodelsof pages 8-9
  16. aiyar2014mitochondrialproteinsorting pages 5-6
  17. magistrati2023drugdroptest pages 5-6
  18. magistrati2023drugdroptest pages 2-3
  19. lefebvrelegendre2001identificationofa pages 1-2
  20. lefebvrelegendre2001identificationofa pages 7-8
  21. schwimmer2006yeastmodelsof pages 6-8
  22. aiyar2014mitochondrialproteinsorting pages 4-5
  23. magistrati2023drugdroptest pages 20-21
  24. https://doi.org/10.1002/prot.20452,
  25. https://doi.org/10.1074/jbc.m009557200,
  26. https://doi.org/10.1016/j.bbamcr.2008.07.001,
  27. https://doi.org/10.1042/bst20130116,
  28. https://doi.org/10.1002/biot.200500053,
  29. https://doi.org/10.1038/ncomms6585,
  30. https://doi.org/10.3390/ijms241310696,
  31. https://doi.org/10.1038/s41467-022-35720-5,